LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 4 of total 4

Search options

  1. Article ; Online: Heterochromatin: an epigenetic point of view in aging.

    Lee, Jong-Hyuk / Kim, Edward W / Croteau, Deborah L / Bohr, Vilhelm A

    Experimental & molecular medicine

    2020  Volume 52, Issue 9, Page(s) 1466–1474

    Abstract: Aging is an inevitable process of life. Defined by progressive physiological and functional loss of tissues and organs, aging increases the risk of mortality for the organism. The aging process is affected by various factors, including genetic and ... ...

    Abstract Aging is an inevitable process of life. Defined by progressive physiological and functional loss of tissues and organs, aging increases the risk of mortality for the organism. The aging process is affected by various factors, including genetic and epigenetic ones. Here, we review the chromatin-specific epigenetic changes that occur during normal (chronological) aging and in premature aging diseases. Taking advantage of the reversible nature of epigenetic modifications, we will also discuss possible lifespan expansion strategies through epigenetic modulation, which was considered irreversible until recently.
    MeSH term(s) Age Factors ; Aging/genetics ; Animals ; Chromatin/genetics ; Chromatin/metabolism ; Epigenesis, Genetic ; Epigenomics/methods ; Gene Expression Regulation ; Heterochromatin/genetics ; Heterochromatin/metabolism ; Histones/metabolism ; Humans ; Longevity
    Chemical Substances Chromatin ; Heterochromatin ; Histones
    Language English
    Publishing date 2020-09-04
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Review
    ZDB-ID 1328915-9
    ISSN 2092-6413 ; 1226-3613 ; 0378-8512
    ISSN (online) 2092-6413
    ISSN 1226-3613 ; 0378-8512
    DOI 10.1038/s12276-020-00497-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 4775: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: Mitochondrial PARP1 regulates NAD

    Lee, Jong-Hyuk / Hussain, Mansoor / Kim, Edward W / Cheng, Shang-Jung / Leung, Anthony K L / Fakouri, Nima Borhan / Croteau, Deborah L / Bohr, Vilhelm A

    Experimental & molecular medicine

    2022  Volume 54, Issue 12, Page(s) 2135–2147

    Abstract: PARPs play fundamental roles in multiple DNA damage recognition and repair pathways. Persistent nuclear PARP activation causes cellular ... ...

    Abstract PARPs play fundamental roles in multiple DNA damage recognition and repair pathways. Persistent nuclear PARP activation causes cellular NAD
    MeSH term(s) Poly ADP Ribosylation ; NAD/metabolism ; Poly(ADP-ribose) Polymerase Inhibitors ; Mitochondria/metabolism ; DNA, Mitochondrial/genetics ; DNA, Mitochondrial/metabolism
    Chemical Substances NAD (0U46U6E8UK) ; Poly(ADP-ribose) Polymerase Inhibitors ; DNA, Mitochondrial
    Language English
    Publishing date 2022-12-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1328915-9
    ISSN 2092-6413 ; 1226-3613 ; 0378-8512
    ISSN (online) 2092-6413
    ISSN 1226-3613 ; 0378-8512
    DOI 10.1038/s12276-022-00894-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 4775: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: CDK2 phosphorylation of Werner protein (WRN) contributes to WRN's DNA double-strand break repair pathway choice.

    Lee, Jong-Hyuk / Shamanna, Raghavendra A / Kulikowicz, Tomasz / Borhan Fakouri, Nima / Kim, Edward W / Christiansen, Louise S / Croteau, Deborah L / Bohr, Vilhelm A

    Aging cell

    2021  Volume 20, Issue 11, Page(s) e13484

    Abstract: Werner syndrome (WS) is an accelerated aging disorder characterized by genomic instability, which is caused by WRN protein deficiency. WRN participates in DNA metabolism including DNA repair. In a previous report, we showed that WRN protein is recruited ... ...

    Abstract Werner syndrome (WS) is an accelerated aging disorder characterized by genomic instability, which is caused by WRN protein deficiency. WRN participates in DNA metabolism including DNA repair. In a previous report, we showed that WRN protein is recruited to laser-induced DNA double-strand break (DSB) sites during various stages of the cell cycle with similar intensities, supporting that WRN participates in both non-homologous end joining (NHEJ) and homologous recombination (HR). Here, we demonstrate that the phosphorylation of WRN by CDK2 on serine residue 426 is critical for WRN to make its DSB repair pathway choice between NHEJ and HR. Cells expressing WRN engineered to mimic the unphosphorylated or phosphorylation state at serine 426 showed abnormal DSB recruitment, altered RPA interaction, strand annealing, and DSB repair activities. The CDK2 phosphorylation on serine 426 stabilizes WRN's affinity for RPA, likely increasing its long-range resection at the end of DNA strands, which is a crucial step for HR. Collectively, the data shown here demonstrate that a CDK2-dependent phosphorylation of WRN regulates DSB repair pathway choice and cell cycle participation.
    MeSH term(s) Cell Cycle/genetics ; Cell Line, Tumor ; Cyclin-Dependent Kinase 2/genetics ; Cyclin-Dependent Kinase 2/metabolism ; DNA/metabolism ; DNA Breaks, Double-Stranded/radiation effects ; DNA End-Joining Repair/genetics ; HEK293 Cells ; Homologous Recombination ; Humans ; Phosphorylation/genetics ; Replication Protein A/metabolism ; Serine/metabolism ; Signal Transduction/genetics ; Transfection ; Werner Syndrome/genetics ; Werner Syndrome/metabolism ; Werner Syndrome Helicase/genetics ; Werner Syndrome Helicase/metabolism
    Chemical Substances RPA1 protein, human ; Replication Protein A ; Serine (452VLY9402) ; DNA (9007-49-2) ; CDK2 protein, human (EC 2.7.11.22) ; Cyclin-Dependent Kinase 2 (EC 2.7.11.22) ; WRN protein, human (EC 3.6.4.12) ; Werner Syndrome Helicase (EC 3.6.4.12)
    Language English
    Publishing date 2021-10-06
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2113083-8
    ISSN 1474-9726 ; 1474-9718
    ISSN (online) 1474-9726
    ISSN 1474-9718
    DOI 10.1111/acel.13484
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 6581: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: Cockayne syndrome group B deficiency reduces H3K9me3 chromatin remodeler SETDB1 and exacerbates cellular aging.

    Lee, Jong-Hyuk / Demarest, Tyler G / Babbar, Mansi / Kim, Edward W / Okur, Mustafa N / De, Supriyo / Croteau, Deborah L / Bohr, Vilhelm A

    Nucleic acids research

    2019  Volume 47, Issue 16, Page(s) 8548–8562

    Abstract: Cockayne syndrome is an accelerated aging disorder, caused by mutations in the CSA or CSB genes. In CSB-deficient cells, poly (ADP ribose) polymerase (PARP) is persistently activated by unrepaired DNA damage and consumes and depletes cellular ... ...

    Abstract Cockayne syndrome is an accelerated aging disorder, caused by mutations in the CSA or CSB genes. In CSB-deficient cells, poly (ADP ribose) polymerase (PARP) is persistently activated by unrepaired DNA damage and consumes and depletes cellular nicotinamide adenine dinucleotide, which leads to mitochondrial dysfunction. Here, the distribution of poly (ADP ribose) (PAR) was determined in CSB-deficient cells using ADPr-ChAP (ADP ribose-chromatin affinity purification), and the results show striking enrichment of PAR at transcription start sites, depletion of heterochromatin and downregulation of H3K9me3-specific methyltransferases SUV39H1 and SETDB1. Induced-expression of SETDB1 in CSB-deficient cells downregulated PAR and normalized mitochondrial function. The results suggest that defects in CSB are strongly associated with loss of heterochromatin, downregulation of SETDB1, increased PAR in highly-transcribed regions, and mitochondrial dysfunction.
    MeSH term(s) Cell Line, Transformed ; Cellular Senescence/genetics ; Chromatin/chemistry ; Chromatin/metabolism ; Cockayne Syndrome/genetics ; Cockayne Syndrome/metabolism ; Cockayne Syndrome/pathology ; DNA/genetics ; DNA/metabolism ; DNA Damage ; DNA Helicases/genetics ; DNA Helicases/metabolism ; DNA Repair Enzymes/genetics ; DNA Repair Enzymes/metabolism ; Fibroblasts/metabolism ; Fibroblasts/pathology ; Gene Expression Regulation ; Histones/genetics ; Histones/metabolism ; Humans ; Methyltransferases/genetics ; Methyltransferases/metabolism ; Mitochondria/metabolism ; Mitochondria/pathology ; Mutation ; NAD/metabolism ; Poly Adenosine Diphosphate Ribose/metabolism ; Poly(ADP-ribose) Polymerases/genetics ; Poly(ADP-ribose) Polymerases/metabolism ; Poly-ADP-Ribose Binding Proteins/genetics ; Poly-ADP-Ribose Binding Proteins/metabolism ; Protein Methyltransferases/genetics ; Protein Methyltransferases/metabolism ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Signal Transduction ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Transcription Initiation Site ; Transcription, Genetic
    Chemical Substances Chromatin ; ERCC8 protein, human ; Histones ; Poly-ADP-Ribose Binding Proteins ; Repressor Proteins ; Transcription Factors ; NAD (0U46U6E8UK) ; Poly Adenosine Diphosphate Ribose (26656-46-2) ; DNA (9007-49-2) ; SUV39H1 protein, human (EC 2.1.1.) ; Methyltransferases (EC 2.1.1.-) ; Protein Methyltransferases (EC 2.1.1.-) ; SETDB1 protein, human (EC 2.1.1.43) ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30) ; DNA Helicases (EC 3.6.4.-) ; ERCC6 protein, human (EC 3.6.4.12) ; DNA Repair Enzymes (EC 6.5.1.-)
    Language English
    Publishing date 2019-07-19
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkz568
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1067: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top